ID A0A087YCS1_POEFO Unreviewed; 531 AA.
AC A0A087YCS1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Serine/threonine-protein kinase OSR1 {ECO:0000256|ARBA:ARBA00040079};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Oxidative stress-responsive 1 protein {ECO:0000256|ARBA:ARBA00042936};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000015824.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000015824.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; AYCK01004982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087YCS1; -.
DR STRING; 48698.ENSPFOP00000015824; -.
DR Ensembl; ENSPFOT00000015846.2; ENSPFOP00000015824.2; ENSPFOG00000015726.2.
DR eggNOG; KOG0582; Eukaryota.
DR GeneTree; ENSGT00940000154621; -.
DR OMA; PDKRPMN; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06610; STKc_OSR1_SPAK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF1; SERINE_THREONINE-PROTEIN KINASE OSR1; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..291
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 314..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 531 AA; 58232 MW; E3AB96133F2469FE CRC64;
MADEQSTQSW TINRDDYELN EVIGSGATAV VQAAYCKPRK EKVAIKRINL EKCQTSMDEL
LKEIQAMSQC HHPNIVSYYT SFVVKDELWL VMKLLSGGSV LDIIKHIISR GEHRNGVLDE
ASIASILKEV LEGLEYLHKN GQIHRDLKAG NILLGDDGSV QIADFGVSAF LATGGDMTRN
KVRKTFVGTP CWMAPEVMEQ VRGYDFKADI WSFGITAIEL ATGAAPYHKY PPMKVLMLTL
QNDPPCLETG VADKETVKKY GKSFRKMISL CLQKDPEKRP TAAELLKHKF FTKAKNNEYL
QEKLLMKGPT ISDRSKKVRR VPGSSGRLHK TEDGGWEWSD DELDEESEEG KAAVAALRSP
RVKDGSQNME LFPPADGATT HLQPPGAAHE RPANLAAAGD EAPPQAATQP ASPSHGPAVQ
DPAASSVPIS LVLRLRNNKK ELNDIRFEFM SGRDSADGVS QELVSAGLVD GRDLVIVAAN
LQKIVDDPQS NKNVTFKLAS GVEESEIPDD VKLIGCIVVN SKDPLLPKRG D
//
